Fusion

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Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

Node Color

colored nodes:query proteins and first shell of interactors

white nodes:second shell of interactors

Node Content

empty nodes:proteins of unknown 3D structure

filled nodes:some 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding each other.

Known Interactions

from curated databases

experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

Others

textmining

co-expression

protein homology

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Gene Fusion

Cooccurence

Coexpression

Experiments

Databases

Textmining

[Homology]

Score

mscL

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell (140 aa)

Predicted Functional Partners:

groS

Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter (97 aa)

0.826

nuoN

NDH-1 subunit N ; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient (480 aa)

0.821

R2601_21812

NADH-quinone oxidoreductase (666 aa)

0.821

ctaB

Heme O synthase ; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group (316 aa)

a tab-delimited file describing the names, domains and annotated functions of the network proteins

Browse interactions in tabular form:

node1

node2

node1 accession

node2 accession

node1 annotation

node2 annotation

score

R2601_01718

ilvD

R2601_01718

R2601_12560

Dihydroxy-acid dehydratase

Dihydroxy-acid dehydratase

0.820

R2601_01718

mscL

R2601_01718

R2601_10614

Dihydroxy-acid dehydratase

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell

0.594

R2601_05298

ilvD

R2601_05298

R2601_12560

Dihydroxy-acid dehydratase

Dihydroxy-acid dehydratase

0.822

R2601_05298

mscL

R2601_05298

R2601_10614

Dihydroxy-acid dehydratase

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell

0.594

R2601_05743

ilvD

R2601_05743

R2601_12560

Dihydroxy-acid dehydratase protein

Dihydroxy-acid dehydratase

0.820

R2601_05743

mscL

R2601_05743

R2601_10614

Dihydroxy-acid dehydratase protein

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell

0.594

R2601_10609

mscL

R2601_10609

R2601_10614

Cation efflux transporter, CDF family protein

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell

0.575

R2601_21647

mscL

R2601_21647

R2601_10614

Phosphogluconate dehydratase

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell

0.594

R2601_21812

ctaB

R2601_21812

R2601_17804

NADH-quinone oxidoreductase

Heme O synthase ; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group

0.863

R2601_21812

groS

R2601_21812

R2601_09902

NADH-quinone oxidoreductase

Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

0.821

R2601_21812

mscL

R2601_21812

R2601_10614

NADH-quinone oxidoreductase

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell

0.821

R2601_21812

nuoN

R2601_21812

R2601_21867

NADH-quinone oxidoreductase

NDH-1 subunit N ; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient

0.991

ctaB

R2601_21812

R2601_17804

R2601_21812

Heme O synthase ; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group

NADH-quinone oxidoreductase

0.863

ctaB

groS

R2601_17804

R2601_09902

Heme O synthase ; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group

Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

0.841

ctaB

mscL

R2601_17804

R2601_10614

Heme O synthase ; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell

0.821

ctaB

nuoN

R2601_17804

R2601_21867

Heme O synthase ; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group

NDH-1 subunit N ; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient

0.825

groS

R2601_21812

R2601_09902

R2601_21812

Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

NADH-quinone oxidoreductase

0.821

groS

ctaB

R2601_09902

R2601_17804

Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

Heme O synthase ; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group

0.841

groS

mscL

R2601_09902

R2601_10614

Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

Large-conductance mechanosensitive channel ; Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell

0.826

groS

nuoN

R2601_09902

R2601_21867

Protein Cpn10 ; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter

NDH-1 subunit N ; NDH-1 shuttles electrons from NADH, via FMN and iron- sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient

0.821

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Network Stats

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Functional enrichments in your networkNote: some enrichments may be expected here (why?)

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Statistical background

For the above enrichment analysis, the following statistical background is assumed: